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Relaxin peptide synthesis

一种松弛素、合成多肽的技术，应用在肽合成领域，能够解决未溶解、困难等问题

Inactive Publication Date: 2012-08-22
PATRAS CHEM & BIOPHARMACEUTICAL LAB
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In addition, difficulties were encountered in forming proper interchain disulfide linkages for RLX1B and RLX2B with the corresponding relaxin A chains due to the insolubility of the B chains during relaxin synthesis leading to undesired precipitation or insolubility of the B chains

Method used

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  • Relaxin peptide synthesis
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Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0096] Human RLX1A, RLX2A, Met(O) 24 -RLX1B and Met(O) 25 - Solid phase synthesis of RLX2B and their protected fragments. General process.

[0097] A1. Preparation of loaded 2-chlorotrityl chloride (CTC) resin; general process:

[0098]CTC-Cl resin (100 g; loading 1.6 mmol / g) was charged into a 2L peptide reactor and swelled with 700 ml DCM at 25°C for 30 min. The resin was drained and then a solution of 100 mmol Fmoc-amino acid and 300 mmol diisopropylethylamine (DIEA) in 500 ml dichloromethane (DCM) was added. The mixture was stirred at a temperature of 25° C. for 2 hours under nitrogen. Then, the active sites remaining on the 2-CTC resin were end-capped by adding 10 ml of MeOH for 1 hour. The resin was evacuated and washed twice with 400 ml of dimethyl formamide (DMF). The resin was evacuated and then treated with 500 mL of 25 vol% piperidine twice for 30 minutes. The resin was then washed four times with 500 ml DMF. The resin was de-swelled by washing 3 times with ...

Embodiment 2

[0117] Linearly reduced RLX1A, RLX2A, Met(O) 24 -RLX1B and Met(O) 25 - Deprotection of RLX2B and their derivatives. General process:

[0118] The protected RLX-chain A (0.01 mmol) obtained as described above in Example 1 was treated with 10 ml of a mixture of TFA / dithiothreitol (DTT) / water (90:5:5) at 5°C Three hours, followed by 1 hour at 15°C. The resulting solution was then concentrated in vacuo and precipitated by the addition of diisopropyl ether, followed by three washes with 10 ml of diisopropyl ether. The obtained solid was then vacuum dried (25°C, 15 Torr) to constant weight. The operation was repeated with RLX chain B protected with an oxidized methionine group.

Embodiment 3

[0120] Single and double loops RLX1A, RLX2A, Met(O) 24 -RLX1B and Met(O) 25 -Deprotection of RLX2B. General process:

[0121] Protected RLX (0.005 mmol) obtained as described above in Example 1 was mixed with 5 ml of TFA / triisopropylsilane (triisopropylsilane, TIPS) / anisole / water (91:4:1:4) The mixture was treated at 5°C for three hours and then at 15°C for 1 hour. The resulting solution was then concentrated in vacuo and precipitated by the addition of diisopropyl ether, followed by three washes with 5 ml of diisopropyl ether. The obtained solid was then vacuum dried (25°C, 15 Torr) to constant weight. Repeat for each chain A and chain B.

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Abstract

A process for producing an insulin type peptide, for example a relaxin, involving oxidizing a methionine residue on a B-chain having cysteine residues and combining the B chain with an A chain having cysteine residues to form a peptide having intermolecular disulphide links and biological activity. Novel synthetic relaxin 1 and methionine oxidized relaxins and Met(O) B-chains having enhanced solubility are disclosed.

Description

[0001] related application [0002] This application claims the benefit of Greek Application No. 20090100310, entitled "Peptide Synthesis", filed 1 June 2009, which is incorporated herein by reference. technical field [0003] The present invention relates to peptide synthesis, especially peptide hormone synthesis. In particular, the present invention relates to the synthesis of insulin family peptides, especially relaxin. Background of the invention [0004] Relaxin (RLX) was discovered in 1926 by Frederick Hisaw [Hisaw, F. (1926) Experimental relaxation of the pubic ligament of the guinea pig. Proc. Soc. Exp. Biol. Med. 23, 661-663], it is Substrate capable of relaxing the pelvic ligament and modulating the function of the female reproductive tract. Peptides of the relaxin family include relaxin-1 (RLX1), relaxin-2 (RLX2) and relaxin-3 (RLX3). Relaxin peptides belong to a larger family of insulin like peptides (INSL). This family of peptides includes insulin and insuli...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/22C07K14/64
CPCA61K38/00A61P9/00A61P17/02A61P21/02A61P35/00A61P37/00C07K14/64C07K14/65
Inventor 科尔奥梅尼斯·K·巴洛斯
Owner PATRAS CHEM & BIOPHARMACEUTICAL LAB
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